This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Copper proteins are common in nature and involved in a variety of biological processes such as respiration, photosynthesis, and redox reactions critical to metabolism. The copper centers are classified according to their spectroscopic properties as type 1, type 2 or type 3. Type 1 copper sites are found in a wide range of electron transfer (ET) proteins, including amicyanin and azurin in bacteria, plastocyanin in plants, and multicopper oxidases such as fungal laccase and human ceruloplasmin. Amicyanin contain a single copper site and plays a critical role in the respiratory chain of certain methylotropic bacteria. It serves as a mediator of electron transfer between methylamine dehydrogenase to cytochrome c-551i. The mutants of amicyanin will be studied to find their role in the electron transfer.